| UniProt ID | RM37_HUMAN | |
|---|---|---|
| UniProt AC | Q9BZE1 | |
| Protein Name | 39S ribosomal protein L37, mitochondrial | |
| Gene Name | MRPL37 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 423 | |
| Subcellular Localization | Mitochondrion . | |
| Protein Description | ||
| Protein Sequence | MALASGPARRALAGSGQLGLGGFGAPRRGAYEWGVRSTRKSEPPPLDRVYEIPGLEPITFAGKMHFVPWLARPIFPPWDRGYKDPRFYRSPPLHEHPLYKDQACYIFHHRCRLLEGVKQALWLTKTKLIEGLPEKVLSLVDDPRNHIENQDECVLNVISHARLWQTTEEIPKRETYCPVIVDNLIQLCKSQILKHPSLARRICVQNSTFSATWNRESLLLQVRGSGGARLSTKDPLPTIASREEIEATKNHVLETFYPISPIIDLHECNIYDVKNDTGFQEGYPYPYPHTLYLLDKANLRPHRLQPDQLRAKMILFAFGSALAQARLLYGNDAKVLEQPVVVQSVGTDGRVFHFLVFQLNTTDLDCNEGVKNLAWVDSDQLLYQHFWCLPVIKKRVVVEPVGPVGFKPETFRKFLALYLHGAA | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 27 | Methylation | LGGFGAPRRGAYEWG CCCCCCCCCCCCCCC | 49.48 | - | |
| 48 | Methylation | SEPPPLDRVYEIPGL CCCCCCCCEEECCCC | 40.37 | 115483767 | |
| 127 | Acetylation | ALWLTKTKLIEGLPE HHHHHHHHHCCCCCH | 49.36 | 19608861 | |
| 127 | Ubiquitination | ALWLTKTKLIEGLPE HHHHHHHHHCCCCCH | 49.36 | 19608861 | |
| 127 | 2-Hydroxyisobutyrylation | ALWLTKTKLIEGLPE HHHHHHHHHCCCCCH | 49.36 | - | |
| 135 | Ubiquitination | LIEGLPEKVLSLVDD HCCCCCHHHHHHHCC | 46.68 | 21890473 | |
| 153 | Glutathionylation | HIENQDECVLNVISH CCCCCCHHHHHHHHH | 5.92 | 22555962 | |
| 172 | Ubiquitination | QTTEEIPKRETYCPV HCCCCCCCCCCCHHH | 69.40 | 21890473 | |
| 189 | Ubiquitination | DNLIQLCKSQILKHP HHHHHHHHHHHHHCH | 54.72 | - | |
| 233 | Ubiquitination | GGARLSTKDPLPTIA CCCCCCCCCCCCCCC | 54.71 | 21906983 | |
| 238 | Phosphorylation | STKDPLPTIASREEI CCCCCCCCCCCHHHH | 36.54 | 20068231 | |
| 249 | Ubiquitination | REEIEATKNHVLETF HHHHHHHHCHHHCCC | 52.70 | - | |
| 320 | Phosphorylation | MILFAFGSALAQARL HHHHHHHHHHHHHHH | 17.41 | 29507054 | |
| 334 | Ubiquitination | LLYGNDAKVLEQPVV HHHCCCCCHHCCCEE | 50.66 | 21890473 | |
| 407 | Ubiquitination | PVGPVGFKPETFRKF CCCCCCCCHHHHHHH | 35.70 | 2190698 | |
| 407 | Acetylation | PVGPVGFKPETFRKF CCCCCCCCHHHHHHH | 35.70 | 26822725 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of RM37_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RM37_HUMAN !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of RM37_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-127, AND MASS SPECTROMETRY. | |